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TitleA methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 18, Page 42-48, Year 2011
Publish dateSep 8, 2010 (structure data deposition date)
AuthorsEsteve, P.O. / Chang, Y. / Samaranayake, M. / Upadhyay, A.K. / Horton, J.R. / Feehery, G.R. / Cheng, X. / Pradhan, S.
External linksNat. Struct. Mol. Biol. / PubMed:21151116
MethodsX-ray diffraction
Resolution1.69 Å
Structure data

PDB-3os5:
SET7/9-Dnmt1 K142me1 complex
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-EDO:
1,2-ETHANEDIOL


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Epigenetic modification / SET domain / Protein lysine methyltransferase / Dnmt1 / lysine mono-methylation / K142

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